Influence of acidic residues and the kink in the active-site helix on the properties of the disulfide oxidoreductase DsbA

Journal of Biological Chemistry

Volumn 272, Issue 1, 1997, Pages 189-195

  Hennecke, Jens ^a   Spleiss, Chantal ^a   Glockshuber, Rudi ^a  

^a ETH ZURICH   (Switzerland)

Author keywords

[No Author keywords available]

Indexed keywords

OXIDOREDUCTASE;

AMINO TERMINAL SEQUENCE; ARTICLE; DISULFIDE BOND; ENZYME ACTIVE SITE; ENZYME CONFORMATION; ESCHERICHIA COLI; GENE INSERTION; NONHUMAN; OXIDATION REDUCTION POTENTIAL; PRIORITY JOURNAL; SEQUENCE ANALYSIS;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; BINDING SITES; DISULFIDES; ESCHERICHIA COLI; GLUTAMIC ACID; GLUTAMINE; HYDROGEN-ION CONCENTRATION; IONS; ISOMERASES; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; OSMOLAR CONCENTRATION; POINT MUTATION; PROTEIN DENATURATION; PROTEIN DISULFIDE-ISOMERASE; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SEQUENCE DELETION; STRUCTURE-ACTIVITY RELATIONSHIP; SUBSTRATE SPECIFICITY; THERMODYNAMICS;

ESCHERICHIA COLI;

EID: 0031033048     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.272.1.189     Document Type: Article

References (51)

1. Bardwell, J. C. A., McGovern, K., and Beckwith, J. (1991) Cell 67, 581-589
2. Kamitani, S., Akiyama, Y., and Ito, K. (1992) EMBO J. 11, 57-62
3. Bardwell, J. C. A., Lee, J.-O., Jander, G., Martin, N., Belin, D., and Beckwith, J. (1993) Proc. Natl. Acad. Sci. U. S. A. 90, 1038-1042
4. Jander, G., Martin, N. L., and Beckwith, J. (1994) EMBO J. 13, 5121-5127
5. Kishigami, S., Kanaya, E., Kikuchi, M., and Ito, K. (1995) J. Biol. Chem. 270, 17072-17074
6. Guilhot, C., Jander, G., Martin, N. L., and Beckwith, J. (1995) Proc. Natl. Acad. Sci. U. S. A. 92, 9895-9899
7. Martin, J. L., Bardwell, J. C. A., and Kuriyan, J. (1993) Nature 365, 464-468
8. Martin, J. L. (1995) Structure 3, 245-250
9. Kraulis, P. J. (1991) J. Appl. Crystallogr. 24, 946-950
10. Katti, S. K., LeMaster, D. M., and Eklund, H. (1990) J. Mol. Biol. 212, 167-184
11. Xia, T.-H., Bushweller, J. H., Sodano, P., Billeter, M., Björnberg, O., Holmgren, A., and Wüthrich, K. (1991) J. Mol. Biol. 221, 1311-1324
12. Wunderlich, M., and Glockshuber, R. (1993) Protein Sci. 2, 717-726
13. Zapun, A., Bardwell, J. C. A., and Creighton, T. E. (1993) Biochemistry 32, 5083-5092
14. Wunderlich, M., Otto, A., Seckler, R., and Glockshuber, R. (1993) Biochemistry 32, 12251-12256
15. Zapun, A., and Creighton, T. E. (1994) Biochemistry 33, 5202-5211
16. Darby, N. J., and Creighton, T. E. (1995) Biochemistry 34, 3576-3587
17. Frech, C., Wunderlich, M., Glockshuber, R., and Schmid, F. X. (1996) EMBO J. 15, 392-398
18. Nelson, J. W., and Creighton, T. E. (1994) Biochemistry 33, 5974-5983
19. Wunderlich, M., Jaenicke, R., and Glockshuber, R. (1993) J. Mol. Biol. 233, 559-566
20. Szajewski, R. P., Whitesides, G. M. (1980) J. Am. Chem. Soc. 102, 2011-2026
21. Grauschopf, U., Winther, J. R., Korber, P., Zander, T., Dallinger, P., and Bardwell, J. C. A. (1995) Cell 83, 947-955
22. Kortemme, T., and Creighton, T. E. (1995) J. Mol. Biol. 253, 799-812
23. Gane, P. J., Freedman, R. B., and Warwicker, J. (1995) J. Mol. Biol. 249, 376-387
24. Warwicker, J., and Gane, P. J. (1996) FEES Lett. 385, 105-108
25. Vieira, J., and Messing, J. (1987) Methods Enzymol. 153, 3-11
26. Kunkel, T. A. (1985) Proc. Natl. Acad. Sci. U. S. A. 82, 488-492
27. Kunkel, T. A., Roberts, J. D., and Zakour, R. A. (1987) Methods Enzymol. 154, 367-382
28. Gill, S. C., and von Hippel, P. H. (1989) Anal. Biochem. 182, 319-326
29. Ellman, G. L. (1959) Arch. Biochem. Biophys. 82, 70-77
30. Dailey, F. E., and Berg, H. C. (1993) Proc. Natl Acad. Sci. U. S. A. 90, 1043-1047
31. Griffey, R. H., and Redfield, A. G. (1985) Biochemistry 24, 817-822
32. Santoro, M. M., and Bolen, D. W. (1988) Biochemistry 27, 8063-8068
33. Rost, J., and Rapoport, S. (1964) Nature 201, 185
34. Otto, A., and Seckler, R. (1991) Eur. J. Biochem. 202, 67-73
35. Lin, T.-Y., and Kim, P. S. (1989) Biochemistry 28, 5282-5287
36. Tanford, C., and Hauenstein, J. D. (1956) J. Am. Chem. Soc. 78, 5287-5291
37. Markwardt, F., and Walsmann, P. (1967) Hoppe-Seyler's Z. Physiol. Chem. 348, 1381-1386
38. Zapun, A., Cooper, L., and Creighton, T. E. (1994) Biochemistry 33, 1907-1914
39. Wunderlich, M., Otto, A., Maskos, K., Mücke, M., Seckler, R., and Glockshuber, R. (1995) J. Mol. Biol. 247, 28-33
40. Prescott, L. M., Harley, J. P., and Klein, D. A. (1990) Microbiology, pp 122-123, William C. Brown Publishers, Dubuque, IA
41. Hol, W. G. J. (1985) Prog. Biophys. Mol. Biol. 45, 149-195
42. Sali, D., Bycroft, M., and Fersht, A. R. (1988) Nature 335, 740-743
43. Serrano, L., and Fersht, A. R. (1989) Nature 342, 296-299
44. Sancho, J., Serrano, L., and Fersht, A. R. (1992) Biochemistry 31, 2253-2258
45. Walter, S., Hubner, B., Hahn, U., and Schmid, F. X. (1995) J. Mol. Biol. 252, 133-143
46. Peek, J. A., and Taylor, R. K. (1992) Proc. Natl. Acad. Sci. U. S. A. 89, 6210-6214
47. Pace, C. N. (1986) Methods Enzymol. 131, 266-280
48. Xia, T.-H., Bushweller, J. H., Sodano, P., Billeter, M., Björnberg, O., Holmgren, A., and Wüthrich, K. (1992) Protein Sci. 1, 310-321
49. Jeng, M.-F., Campbell, A. P., Begley, T., Holmgren, A., Case, D. A., Wright, P. E., and Dyson, H. J. (1994) Structure 2, 853-868
50. Qin, J., Clore, G. M., and Gronenborn, A. M. (1994) Structure 2, 503-522
51. Weichsel, A., Gasdaska, J. R., Powis, G., and Montfort, W. R. (1996) Structure 4, 735-751